The subunit structure of nitrite reductase purified from the denitrifier Achromobacter cycloclastes |
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Authors: | Inatomi K |
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Affiliation: | Advanced Technology R&D Center, Mitsubishi Electric Corp., Hyogo, Japan. inatomi@bio.crl.melco.co.jp |
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Abstract: | The copper-containing nitrite reductase of Achromobacter cycloclastes has been considered to be a homotrimer with three identical subunits both in the crystal and in solution. In this study, however, the enzyme was found to be a heterotrimer consisting of two subunits with molecular masses of 37 kDa and 36.2 kDa, and the 37 kDa subunit was 6 amino acid residues longer than the smaller subunit. Signal-peptide cleavage sites in its N-terminal region are discussed. |
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